FisR activates σ54‐dependent transcription of sulfide‐oxidizing genes in Cupriavidus pinatubonensis JMP134. Issue 3 (29th June 2017)
- Record Type:
- Journal Article
- Title:
- FisR activates σ54‐dependent transcription of sulfide‐oxidizing genes in Cupriavidus pinatubonensis JMP134. Issue 3 (29th June 2017)
- Main Title:
- FisR activates σ54‐dependent transcription of sulfide‐oxidizing genes in Cupriavidus pinatubonensis JMP134
- Authors:
- Li, Huanjie
Li, Juan
Lü, Chuanjuan
Xia, Yongzhen
Xin, Yufeng
Liu, Honglei
Xun, Luying
Liu, Huaiwei - Abstract:
- Summary: Some heterotrophic bacteria are able to oxidize sulfide (H2 S, HS − and S 2− ) to sulfite and thiosulfate via polysulfide. The genes coding for the oxidation enzymes in Cupriavidus pinatubonensis JMP134 have recently been identified; however, their regulation is unknown. A regulator gene is adjacent to the operon of the sulfide‐oxidizing genes, encoding a σ 54 ‐dependent transcription factor (FisR) with three domains: an R domain, an AAA+ domain and a DNA‐binding domain. Here it is reported that the regulator responds to the presence of sulfide and activates the sulfide‐oxidizing genes. FisR binds to its cognate operator at −114 to −135 bp of the transcription start of the operon. When polysulfide reacts with the R domain of FisR through the three conserved cysteine residues (C53, C64 and C71), FisR activates the expression of the operon. FisR is highly sensitive to polysulfide, activating σ 54 ‐dependent transcription of sulfide‐oxidizing genes for sulfide removal. Further, sequence analysis indicates that FisR‐type regulators are relatively common for controlling sulfide‐oxidizing genes under sulfide stress in the Proteobacteria. Abstract : Heterotrophic bacteria can oxidize H2 S to sulfite and thiosulfate with sulfide:quinone oxidoreductase and persulfide dioxygenase. Some of them use σ 54 ‐dependent transcriptional factor FisR to sense sulfide (H2 S, HS −, and S 2− ) stress and activate the sulfide‐oxidizing genes. Polysulfide, a sulfide oxidation intermediate,Summary: Some heterotrophic bacteria are able to oxidize sulfide (H2 S, HS − and S 2− ) to sulfite and thiosulfate via polysulfide. The genes coding for the oxidation enzymes in Cupriavidus pinatubonensis JMP134 have recently been identified; however, their regulation is unknown. A regulator gene is adjacent to the operon of the sulfide‐oxidizing genes, encoding a σ 54 ‐dependent transcription factor (FisR) with three domains: an R domain, an AAA+ domain and a DNA‐binding domain. Here it is reported that the regulator responds to the presence of sulfide and activates the sulfide‐oxidizing genes. FisR binds to its cognate operator at −114 to −135 bp of the transcription start of the operon. When polysulfide reacts with the R domain of FisR through the three conserved cysteine residues (C53, C64 and C71), FisR activates the expression of the operon. FisR is highly sensitive to polysulfide, activating σ 54 ‐dependent transcription of sulfide‐oxidizing genes for sulfide removal. Further, sequence analysis indicates that FisR‐type regulators are relatively common for controlling sulfide‐oxidizing genes under sulfide stress in the Proteobacteria. Abstract : Heterotrophic bacteria can oxidize H2 S to sulfite and thiosulfate with sulfide:quinone oxidoreductase and persulfide dioxygenase. Some of them use σ 54 ‐dependent transcriptional factor FisR to sense sulfide (H2 S, HS −, and S 2− ) stress and activate the sulfide‐oxidizing genes. Polysulfide, a sulfide oxidation intermediate, is the real signal instead of sulfide. … (more)
- Is Part Of:
- Molecular microbiology. Volume 105:Issue 3(2017)
- Journal:
- Molecular microbiology
- Issue:
- Volume 105:Issue 3(2017)
- Issue Display:
- Volume 105, Issue 3 (2017)
- Year:
- 2017
- Volume:
- 105
- Issue:
- 3
- Issue Sort Value:
- 2017-0105-0003-0000
- Page Start:
- 373
- Page End:
- 384
- Publication Date:
- 2017-06-29
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.13725 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2914.xml